CRDL1_RAT
ID CRDL1_RAT Reviewed; 447 AA.
AC Q76LD0;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Chordin-like protein 1;
DE AltName: Full=Kohjirin;
DE AltName: Full=Neuralin-1;
DE AltName: Full=Neurogenesin-1;
DE AltName: Full=Ventroptin;
DE Flags: Precursor;
GN Name=Chrdl1; Synonyms=Kjr, Ng1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14684875; DOI=10.1523/jneurosci.23-37-11732.2003;
RA Ueki T., Tanaka M., Yamashita K., Mikawa S., Qiu Z., Maragakis N.J.,
RA Hevner R.F., Miura N., Sugimura H., Sato K.;
RT "A novel secretory factor, neurogenesin-1, provides neurogenic
RT environmental cues for neural stem cells in the adult hippocampus.";
RL J. Neurosci. 23:11732-11740(2003).
CC -!- FUNCTION: Seems to antagonize the function of BMP4 by binding to it and
CC preventing its interaction with receptors. Alters the fate commitment
CC of neural stem cells from gliogenesis to neurogenesis. Contributes to
CC neuronal differentiation of neural stem cells in the brain by
CC preventing the adoption of a glial fate. May play a crucial role in
CC dorsoventral axis formation. May play a role in embryonic bone
CC formation. Plays a role during anterior segment eye development (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:14684875}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in neurogenic regions of
CC the embryonic brain. {ECO:0000269|PubMed:14684875}.
CC -!- CAUTION: The sequence shown has an N-terminus according to mammalian
CC orthologs. The original sequence from PubMed:14684875 gives a longer N-
CC terminus and suggests a signal sequence of 97 AA. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD06447.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB080636; BAD06447.1; ALT_INIT; mRNA.
DR RefSeq; NP_955796.1; NM_199502.1.
DR AlphaFoldDB; Q76LD0; -.
DR SMR; Q76LD0; -.
DR STRING; 10116.ENSRNOP00000006008; -.
DR GlyGen; Q76LD0; 2 sites.
DR PhosphoSitePlus; Q76LD0; -.
DR PaxDb; Q76LD0; -.
DR PRIDE; Q76LD0; -.
DR GeneID; 363455; -.
DR KEGG; rno:363455; -.
DR CTD; 91851; -.
DR RGD; 735215; Chrdl1.
DR eggNOG; ENOG502QQFQ; Eukaryota.
DR InParanoid; Q76LD0; -.
DR OrthoDB; 454087at2759; -.
DR PhylomeDB; Q76LD0; -.
DR Reactome; R-RNO-201451; Signaling by BMP.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q76LD0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0036122; F:BMP binding; ISO:RGD.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; ISO:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001709; P:cell fate determination; IMP:RGD.
DR GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISO:RGD.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IMP:RGD.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
DR InterPro; IPR045717; CHRDL1/2.
DR InterPro; IPR045716; CHRDL_1/2_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46303; PTHR46303; 1.
DR Pfam; PF19548; CHRDL_1_2_C; 1.
DR Pfam; PF00093; VWC; 3.
DR SMART; SM00214; VWC; 3.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 3.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Glycoprotein; Neurogenesis;
KW Osteogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..447
FT /note="Chordin-like protein 1"
FT /id="PRO_0000223676"
FT DOMAIN 30..95
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 108..174
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 253..318
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 199..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 174..176
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 50560 MW; 5B76AC14008C0838 CRC64;
MEGIKYIASL VFFFVFLEAS KTEPVKHSET YCMFQDKKYR VGEKWHPYLE PYGLVYCVNC
ICSENGNVLC SRVRCPTLHC LSPVHIPHLC CPRCPDSLPP MNSKVTSKSC EYNGTTYQHG
ELFIAEGLFQ NRQPNQCSQC SCSEGNVYCG LKTCPKLTCA FPVSVPDSCC RVCRGDGELS
WEHSDADIFR QPANREARHS YLRSPYDPPP SRQAGGLPRF AGSRSHRGAV IDSQQASGTI
VQIVINNKHK HGQVCVSNGK TYSHGESWHP NLRAFGIVEC VLCTCNVTKQ ECKKIHCPNR
YPCKYPQKLD GKCCKVCPEE PPSQNFDSKG SFCGEETMPV YEAVLVEDGE TARKVALETE
KPPQVEVHVW TIRKGILQHF HIEKISKEMF GGLHHFKLVT RTTMNQWKIF AEGEAQLSQM
CSSRVCRTEL EDLVQVLYLE RPEKDHC
